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Leukosialin, a major sialoglycoprotein on human leukocytes as differentiation antigens.
Most blood cells derived from the bone-marrow are known to possess only a limited number of heavily sialylated glycoproteins. We have recently isolated a major sialoglycoprotein on leukocytes and found that this glycoprotein, termed leukosialin, is ubiquitously present on various human leukocytes, granulocytes, monocytes/macrophages and T- and B-lymphocytes. Our studies showed that leukosialin is significantly glycosylated by O-linked oligosaccharides (90 chains/molecule). The structures of those O-linked oligosaccharides are characteristic to each cell lineage and maturation stage. The polypeptide portion of these molecules are, however, apparently the same, with a molecular size of 52 KDa. So it will be interesting to explore the possibility that leukosialin expresses different functions by having different O-glycosylation in a variety of hematopoietic cells.
PMID: 2950285 [PubMed - indexed for MEDLINE]
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Cited by 6 PubMed Central articles
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Characterization of porcine intestinal receptors for the K88ac fimbrial adhesin of Escherichia coli as mucin-type sialoglycoproteins.
Erickson AK, Baker DR, Bosworth BT, Casey TA, Benfield DA, Francis DH.
Infect Immun. 1994 Dec; 62(12):5404-10.
[Infect Immun. 1994]
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Regulation of susceptibility and cell surface receptor for the B-lymphotropic papovavirus by N glycosylation.
Keppler OT, Herrmann M, Oppenländer M, Meschede W, Pawlita M.
J Virol. 1994 Nov; 68(11):6933-9.
[J Virol. 1994]
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Monoclonal antibodies to leucosialin (CD43) induce homotypic aggregation of the human mast cell line HMC-1: characterization of leucosialin on HMC-1 cells.
Weber S, Ruh B, Dippel E, Czarnetzki BM.
Immunology. 1994 Aug; 82(4):638-44.
[Immunology. 1994]
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